Browsing by Author "Mao, S. J. T."
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Item type:Item, A novel two-dimentional gel electrophoresis for studing the cress-linking between beta-Lactoglobulin and milk proteins(2005) ;Chen, W. L. ;Huang, M. T. ;Mao, S. J. T. ;交大名義發表National Chiao Tung UniversityItem type:Item, A novel two-dimentional gel electrophoresis for studing the cress-linking between beta-Lactoglobulin and milk proteins(2005) ;Chen, W. L. ;Huang, M. T. ;Mao, S. J. T. ;交大名義發表National Chiao Tung UniversityItem type:Item, A novel two-dimentional gel electrophoresis for studing the cress-linking between beta-Lactoglobulin and milk proteins(2005-01-01) ;Chen, W. L. ;Huang, M. T. ;Mao, S. J. T. ;交大名義發表National Chiao Tung UniversityItem type:Item, Antioxidant nature of bovine milk beta-lactoglobulin(2007-02-01) ;Liu, H. C. ;Chen, W. L. ;Mao, S. J. T. ;生物科技學系Department of Biological Science and TechnologyHeating is necessary for processing milk in the dairy industry, which evidently produces a conformational change in beta-lactoglobulin (beta-LG). beta-Lactoglobulin, a major protein that accounts for approximately 10 to 15% of total milk proteins, is a globular protein consisting of 162 AA with a relative molecular mass of 18.4 kDa. The purpose of the present study was to determine the antioxidant role of beta-LG in milk and the possible mechanism involved. We showed that beta-LG is a mild antioxidant whose potency is less than that of vitamin E and probucol (the latter being an antioxidant used for clinical therapy). The conversion of the beta-LG monomer to dimer was responsible, in part, for the mode of action in protecting low- density lipoproteins against copper-induced oxidation. Cross-linking the free thiol groups of beta-LG by heating (100 degrees C for 2 min), or chemically modifying the beta-LG by carboxymethylation to block the thiol groups resulted in a substantial loss of antioxidant activity. The data suggest that Cys-121 plays an essential role in the antioxidant nature of beta-LG. By using an anti-LG antibody affinity column to deplete the beta-LG from milk, we observed from the lost antioxidant activity that beta-LG contributes approximately 50% of the total activity. Because beta-LG is extremely sensitive to thermal denaturation, to maintain its antioxidant nature, dairy products consumed daily should not be overheated in order to maintain its antioxidant nature.Item type:Item, Distinguish between native and thermally denatured 5-lactoglobulin using a monoclonal antibody as a probe.(2005) ;Mao, S. J. T. ;Chen, W. L. ;Yang, M. C. ;Liu, W. T.交大名義發表Item type:Item, Distinguish between native and thermally denatured beta-lactoglobulin using a monoclonal antibody as a probe(2005) ;Mao, S. J. T. ;Chen, W. L. ;Yang, M. C. ;Liu, W. T.交大名義發表Item type:Item, Haptoglobin 2-2 Genotype Associates With Poor Acute Respiratory Distress Syndrome Outcomes(2013) ;Chen, C. -Y. ;Mao, S. J. T. ;Yang, K. -Y. ;交大名義發表National Chiao Tung UniversityItem type:Item, Residues 69-74 of beta-lactoglobulin are responsible for a monoclonal antibody binding to thermal denatured lactoglobulin(2005) ;Song, C. Y. ;Yang, M. C. ;Mao, S. J. T. ;交大名義發表National Chiao Tung UniversityItem type:Item, Residues 69-74 of beta-lactoglobulin are responsible for a monoclonal antibody binding to thermal denatured lactoglobulin.(2005) ;Song, C. Y. ;Yang, M. C. ;Mao, S. J. T. ;交大名義發表National Chiao Tung University